1YAX
Cystal structure Analysis of S.typhimurium PhoQ sensor domain with Calcium
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000160 | biological_process | phosphorelay signal transduction system |
A | 0004673 | molecular_function | protein histidine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0016020 | cellular_component | membrane |
A | 0018106 | biological_process | peptidyl-histidine phosphorylation |
A | 0046872 | molecular_function | metal ion binding |
B | 0000160 | biological_process | phosphorelay signal transduction system |
B | 0004673 | molecular_function | protein histidine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0016020 | cellular_component | membrane |
B | 0018106 | biological_process | peptidyl-histidine phosphorylation |
B | 0046872 | molecular_function | metal ion binding |
C | 0000160 | biological_process | phosphorelay signal transduction system |
C | 0004673 | molecular_function | protein histidine kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0016020 | cellular_component | membrane |
C | 0018106 | biological_process | peptidyl-histidine phosphorylation |
C | 0046872 | molecular_function | metal ion binding |
D | 0000160 | biological_process | phosphorelay signal transduction system |
D | 0004673 | molecular_function | protein histidine kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0016020 | cellular_component | membrane |
D | 0018106 | biological_process | peptidyl-histidine phosphorylation |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA D 1001 |
Chain | Residue |
A | GLU154 |
A | HIS192 |
A | HOH1009 |
A | HOH1053 |
D | GLU123 |
D | GLU154 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 1002 |
Chain | Residue |
D | GLU123 |
A | GLU154 |
A | HOH1027 |
A | HOH1048 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA C 1003 |
Chain | Residue |
B | GLU123 |
B | HOH1013 |
C | GLU123 |
C | GLU154 |
C | HOH1023 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 1004 |
Chain | Residue |
B | GLU123 |
B | GLU154 |
C | GLU154 |
C | HIS192 |
C | HOH1007 |
C | HOH1008 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA C 1005 |
Chain | Residue |
C | ASP149 |
C | LYS186 |
C | SER188 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA A 1006 |
Chain | Residue |
A | ASP149 |
A | LYS186 |
A | SER188 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CA A 1007 |
Chain | Residue |
A | GLU121 |
A | ILE122 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ASP151 | |
A | ASP152 | |
B | ASP151 | |
B | ASP152 | |
C | ASP151 | |
C | ASP152 | |
D | ASP151 | |
D | ASP152 |